Cloning, sequencing, and characterization of CYP1A1 cDNA from leaping mullet (Liza Saliens) liver and implications for the potential functions of its conserved amino acids

2001 ◽  
Vol 15 (5) ◽  
pp. 243-255 ◽  
Author(s):  
Alaattin Sen ◽  
Chin-Hwa Hu ◽  
Ena Urbach ◽  
Jun-Lan Wang-Buhler ◽  
Yea-Huey Yang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Potential Functions ◽  
Liza Saliens ◽  
Conserved Amino Acids

scholarly journals Molecular cloning and characterization of ornithine decarboxylase cDNA of the nematode Panagrellus redivivus

1995 ◽  
Vol 308 (2) ◽  
pp. 635-640 ◽  
Author(s):  
H von Besser ◽  
G Niemann ◽  
B Domdey ◽  
R D Walter
Keyword(s):  
Amino Acids ◽  
Active Sites ◽  
Cdna Clones ◽  
Degenerate Primers ◽  
Calculated Molecular Mass ◽  
Panagrellus Redivivus ◽  
Free Living Nematode ◽  
Mixed Stage ◽  
Conserved Amino Acids

In a PCR with degenerate primers encoding highly conserved amino acids within ornithine decarboxylases (ODCs) of several organisms, a fragment of the ODC gene of the free-living nematode Panagrellus redivivus was isolated. Northern blot analysis revealed a single 1.7 kb transcript in a mixed-stage population of animals. From this RNA source, a cDNA library was constructed and screened with the PCR fragment. Several cDNA clones were isolated, one of which encodes the complete 435-amino-acid ODC enzyme with a calculated molecular mass of 47.1 kDa. The P. redivivus ODC possesses 126 of the 136 highly conserved amino acids in the enzymes from fungi, invertebrates and vertebrates. Functional amino acids are conserved, suggesting that the two active sites of the P. redivivus ODC are formed at the interface of a homodimer, as described for mammalian ODCs.

scholarly journals Characterization of mutants of three highly conserved amino acids in microsomal cytochrome P450 2B4

2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Lucy Waskell ◽  
Haoming Zhang ◽  
Sang‐Choul Im ◽  
Roman Davydov ◽  
Brian Hoffman
Keyword(s):  
Amino Acids ◽  
Cytochrome P450 ◽  
Microsomal Cytochrome ◽  
Cytochrome P450 2B4 ◽  
Microsomal Cytochrome P450 ◽  
Conserved Amino Acids

Post-proline endopeptidase, further characterization of the enzyme from pig kidneys

1984 ◽  
Vol 49 (8) ◽  
pp. 1846-1853 ◽  
Author(s):  
Karel Hauzer ◽  
Tomislav Barth ◽  
Linda Servítová ◽  
Karel Jošt
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Relative Molecular Mass ◽  
Enzyme Molecule ◽  
Thiol Compounds ◽  
Modified Method ◽  
N Terminus

A post-proline endopeptidase (EC 3.4.21.26) was isolated from pig kidneys using a modified method described earlier. The enzyme was further purified by ion exchange chromatography on DEAE-Sephacel. The final product contained about 95% of post-proline endopeptidase. The enzyme molecule consisted of one peptide chain with a relative molecular mass of 65 600 to 70 000, containing a large proportion of acidic and alifatic amino acids (glutamic acid, aspartic acid and leucine) and the N-terminus was formed by aspartic acid or asparagine. In order to prevent losses of enzyme activity, thiol compounds has to be added.

Sign in / Sign up

Export Citation Format

Share Document